Pancreatic lipase is released into the duodenum through the duct system of the pancreas. Usually, its concentration of serum is very low. Found in the intestinal lumen, the basic pancreatic lipase used to digest the fat droplets is Streapsin. Under extreme disruption of pancreatic function, such as pancreatitis, the pancreas may begin to autolyse and release pancreatic enzymes into serum. Thus, through measurement of serum concentration of pancreatic lipase, pancreatitis can be diagnosed.
Monday, December 29, 2008
Pancreatic lipase is a digestive enzyme secreted by the pancreas that breaks apart fat molecules through hydrolysis. Bile salts secreted from the liver and stored in the gallbladder are released into the duodenum where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal. This protein belongs to pancreatic lipase family. Unlike some pancreatic enzymes like trypsin, which are first secreted in the inactive form of trypsinogen, pancreatic lipase is secreted as an active enzyme.